Literature DB >> 11052488

The pentapeptide NKISK affects collagen fibril interactions in a vertebrate tissue.

L E Dahners1, G E Lester, P Caprise.   

Abstract

The pentapeptide NKISK has been reported to inhibit the binding of decorin, a proteoglycan on the surface of collagen fibrils, to fibronectin, a tissue adhesion molecule. Because of our interest in fibril-fibril binding as it relates to changes in length of ligament or tendon (during growth or contracture), we investigated the potential of this peptide to dissociate fibrils. The peptide permitted the release of intact fibrils into suspension for examination under the electron microscope (which has not previously been possible in mature vertebrate tissues).

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Year:  2000        PMID: 11052488     DOI: 10.1002/jor.1100180404

Source DB:  PubMed          Journal:  J Orthop Res        ISSN: 0736-0266            Impact factor:   3.494


  3 in total

1.  Tendon creep is potentiated by NKISK and relaxin which produce collagen fiber sliding.

Authors:  Mark L Wood; William N Luthin; Gayle E Lester; Laurence E Dahners
Journal:  Iowa Orthop J       Date:  2003

Review 2.  The pathogenesis of tendinopathy: balancing the response to loading.

Authors:  S Peter Magnusson; Henning Langberg; Michael Kjaer
Journal:  Nat Rev Rheumatol       Date:  2010-03-23       Impact factor: 20.543

3.  Mechanical properties of the compass depressors of the sea-urchin Paracentrotus lividus (Echinodermata, Echinoidea) and the effects of enzymes, neurotransmitters and synthetic tensilin-like protein.

Authors:  Iain C Wilkie; Dario Fassini; Emanuele Cullorà; Alice Barbaglio; Serena Tricarico; Michela Sugni; Luca Del Giacco; M Daniela Candia Carnevali
Journal:  PLoS One       Date:  2015-03-18       Impact factor: 3.240

  3 in total

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